ArticleLife science alliance2018
Molecular analysis of human Ero1 reveals novel regulatory mechanisms for oxidative protein folding.
Article in Life science alliance, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Mapping the membrane-enriched proteome of recombinant Chinese hamster ovary cells following induction of endoplasmic reticulum stress.Biotechnology letters · 2026Article
- The role of glycoproteins in autophagy and apoptosis in colorectal cancer: A scoping review.Medical oncology (Northwood, London, England) · 2026Article
- Thiol Isomerases: Enzymatic Mechanisms, Models of Oxidation, and Antagonism by Galloylated Polyphenols.Antioxidants (Basel, Switzerland) · 2025Review
- Cnidarian toxins: omics approaches and recombinant proteins.The journal of venomous animals and toxins including tropical diseases · 2025Article
- Unfolded protein response modulates the effects of GHRH antagonists in experimental models ofTissue barriers · 2025Article
- Thioredoxin Domain Containing 5 (TXNDC5): Friend or Foe?Current issues in molecular biology · 2024Review
- Biochemical analysis of Komagataella phaffii oxidative folding proposes novel regulatory mechanisms of disulfide bond formation in yeast.Scientific reports · 2023Article
- Production of neutralizing antibody fragment variants in the cytoplasm of E. coli for rapid screening: SARS-CoV-2 a case study.Scientific reports · 2023Article
- Protein quality control and aggregation in the endoplasmic reticulum: From basic to bedside.Frontiers in cell and developmental biology · 2023Review
- ER-phagy in the Occurrence and Development of Cancer.Biomedicines · 2022Review
- The regulation of Hypoxia-Inducible Factor-1 (HIF-1alpha) expression by Protein Disulfide Isomerase (PDI).PloS one · 2021Article
- Strategies for Heterologous Expression, Synthesis, and Purification of Animal Venom Toxins.Frontiers in bioengineering and biotechnology · 2021Review
- Non-native proteins inhibit the ER oxidoreductin 1 (Ero1)-protein disulfide-isomerase relay when protein folding capacity is exceeded.The Journal of biological chemistry · 2020Article
- Kinetic characterisation of Erv1, a key component for protein import and folding in yeast mitochondria.The FEBS journal · 2020Article
- Production of Extracellular Matrix Proteins in the Cytoplasm ofInternational journal of molecular sciences · 2020Article
- The Role of ERO1α in Modulating Cancer Progression and Immune Escape.Journal of cancer immunology · 2020Article
- Regulation of plant ER oxidoreductin 1 (ERO1) activity for efficient oxidative protein folding.The Journal of biological chemistry · 2019Article
- The three-dimensional structure of an H-superfamily conotoxin reveals a granulin fold arising from a common ICK cysteine framework.The Journal of biological chemistry · 2019Article
- Ero1-Mediated Reoxidation of Protein Disulfide Isomerase Accelerates the Folding of Cone Snail Toxins.International journal of molecular sciences · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oxidative protein folding in the ER is driven mainly by oxidases of the endoplasmic reticulum oxidoreductin 1 (Ero1) family. Their action is regulated to avoid cell stress, including hyperoxidation. Previously published regulatory mechanisms are based on the rearrangement of active site and regulatory disulfides. In this study, we identify two novel regulatory mechanisms. First, both human Ero1 isoforms exist in a dynamic mixed disulfide complex with protein disulfide isomerase, which involves cysteines (Cys166 in Ero1α and Cys165 in Ero1β) that have previously been regarded as being nonfunctional. Second, our kinetic studies reveal that Ero1 not only has a high affinity for molecular oxygen as the terminal acceptor of electrons but also that there is a high cooperativity of binding (Hill coefficient >3). This allows Ero1 to maintain high activity under hypoxic conditions, without compromising cellular viability under hyper-hypoxic conditions. These data, together with novel mechanistic details of differences in activation between the two human Ero1 isoforms, provide important new insights into the catalytic cycle of human Ero1 and how they have been fine-tuned to operate at low oxygen concentrations.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.